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MFG-E8: a model of multiple binding modes associated with ps-binding proteins.

Tiffany Suwatthee1, Daniel Kerr1,2,3, Sofiya Maltseva1

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This study reveals milk fat globule EGF factor 8 (MFG-E8) exhibits three distinct binding modes to lipid membranes, influenced by phosphatidylserine (PS) availability and membrane packing. This advances understanding of membrane protein interactions.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Membrane-binding proteins typically exhibit a two-state binding model (bound/unbound).
  • A single binding interface can display multiple binding modes, but these are difficult to distinguish.
  • Milk fat globule EGF factor 8 (MFG-E8) binds phosphatidylserine (PS), a marker for cellular apoptosis and malignancy.

Purpose of the Study:

  • To investigate the binding modes of MFG-E8 to lipid membranes.
  • To elucidate the factors influencing MFG-E8's binding affinity and cooperativity.
  • To develop a new model for analyzing multi-modal protein-lipid interactions.

Main Methods:

  • Utilized a model system of lipid vesicles with varying phosphatidylserine (PS) mole fractions.
  • Employed tryptophan fluorescence spectral shift assays to measure binding affinity.
  • Applied X-ray reflectivity experiments to assess membrane packing effects.

Main Results:

  • Identified three distinct binding modes for MFG-E8, each correlating with a specific number of PS lipids.
  • Demonstrated that the availability of negatively charged lipids enhances MFG-E8's binding cooperativity.
  • Found that membrane packing influences MFG-E8's binding modes.

Conclusions:

  • MFG-E8 exhibits complex, multi-modal binding to lipid membranes, not a simple two-state interaction.
  • Electrostatic interactions with PS lipids and membrane packing are key determinants of MFG-E8 binding.
  • The developed methods can be applied to study other membrane-binding proteins and their interactions with membrane attributes.